Exploring a new serine protease from Cucumis sativus L

Area of Science:

• Biochemistry
• Physiology

Background:

• Hemostasis relies on the blood coagulation cascade, a complex process involving sequential protease activation.
• Proteases play a critical role in regulating blood clotting and fibrinolysis.

Purpose of the Study:

• To investigate the potential of aqueous fruit extract of Cucumis sativus L. (AqFEC) in modulating the blood coagulation cascade.
• To identify and characterize protease activities within AqFEC.

Main Methods:

• Casein hydrolysis assays to detect proteolytic activity.
• Casein zymography to identify protease molecular weight.
• Fibrinogenolytic activity assessment using Aα, Bβ, and γ subunits.
• Plasma clotting time reduction assay.

Main Results:

• AqFEC demonstrated dose-dependent casein hydrolysis, indicating protease presence.
• Casein zymography revealed two high molecular weight proteases, sensitive to phenyl methyl sulphonyl fluoride, suggesting serine protease activity.
• AqFEC hydrolyzed fibrinogen Aα and Bβ subunits but not the γ subunit.
• AqFEC significantly reduced plasma clotting time by 87.65%.

Conclusions:

• The study identified serine protease(s) in AqFEC with fibrinogenolytic activity.
• AqFEC's ability to reduce clotting time suggests potential applications in hemostasis and wound healing.